Efficient production of N-terminally truncated biologically active human interleukin-6 by Bacillus brevis |
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Authors: | Shiga Y Maki M Ohta T Tokishita S Okamoto A Tsukagoshi N Udaka S Konishi A Kodama Y Ejima D Matsui H Yamagata H |
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Affiliation: | School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Japan. |
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Abstract: | cDNAs encoding human interleukin 6 (hIL-6) and its variants lacking the N-terminal Pro and Pro-Val-Pro-Pro, respectively, were expressed in Bacillus brevis by using the signal peptide fusion approach. The presence of Pro at the N-terminus of the mature protein hindered the action of the Bacillus brevis signal peptidase. hIL-6 lacking the N-terminal Pro-Val-Pro-Pro was most efficiently secreted in a biologically active form and accumulated in the culture medium to a level of 200 mg per liter, which is the highest level reported for the bacterial secretion of hIL-6. |
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